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P50718 (LYS_TRINI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismTrichoplusia ni (Cabbage looper)
Taxonomic identifier7111 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaePlusiinaeTrichoplusia

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

Catalytic activity

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionlysozyme activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 141121Lysozyme
PRO_0000018509

Sites

Active site531 By similarity
Active site711 By similarity

Amino acid modifications

Disulfide bond27 ↔ 141 By similarity
Disulfide bond48 ↔ 131 By similarity
Disulfide bond83 ↔ 97 By similarity
Disulfide bond93 ↔ 111 By similarity

Sequences

Sequence LengthMass (Da)Tools
P50718 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 64510118422161E8

FASTA14116,271
        10         20         30         40         50         60 
MQKLRVFLLA LAALCISCEA KYFATNCELV HELRRQGFPE DKMRDWVCLI QNESGRNTSK 

        70         80         90        100        110        120 
MGTINKNGSR DYGLFQINDK YWCSKTSTPG KDCNVTCAEM LLDDITKASK CAKKIYKRHK 

       130        140 
FQAWYGWRNH CQGTLPDISK C 

« Hide

References

[1]"PCR differential display of immune gene expression in Trichoplusia ni."
Kang D., Liu G., Gunne H., Steiner H.
Insect Biochem. Mol. Biol. 26:177-184(1996) [PubMed: 8882660] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38782 mRNA. Translation: AAB41353.1.

3D structure databases

ProteinModelPortalP50718.
SMRP50718. Positions 25-141.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYS_TRINI
AccessionPrimary (citable) accession number: P50718
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 31, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families